Codimension-2 black hole solutions on a thin 3-brane and their extension into the bulk

In this talk we discuss black hole solutions in six-dimensional gravity with a Gauss- Bonnet term in the bulk and an induced gravity term on a thin 3-brane of codimension-2. It is shown that these black holes can be localized on the 3-brane, and they can further be extended into the bulk by a warp function. These solutions have regular horizons and no other curvature singularities appear apart from the string-like ones. The projection of the Gauss-Bonnet term on the brane imposes a constraint relation which requires the presence of matter in the extra dimensions, in order to sustain our solutions.Comment: 9 pages, Talk given at the conference "NEB-XIII:Recent developments in gravity" held at Thessaloniki, Greece in June 200

Purification and characterisation of a cysteine-rich 11.5 kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas

Extracts of the granular haemocytes of Carcinus maenas were subjected to ion-exchange chromatography and reverse-phase (RP)-HPLC to investigate the presence of an antibacterial protein of approximate to 11 kDa, This protein was isolated, characterized and subjected to partial amino acid sequence analysis. It was found by mass spectrometry to have a molecular mass of 11 534 Da, to be cationic and hydrophobic and active only against marine Gram-positive bacteria. In addition its activity is stable after heating to 100 degrees C and is retained at concentrations as low as 10 mu g.mL(-1). It has an unusual amino acid sequence, unlike any known antibacterial peptide described in the literature but bears a consensus disulphide domain signature, indicating that it might be a member of the four-disulphide core proteins. Partial cDNA sequence data has been obtained.</p

Purification and characterisation of a cysteine-rich 11.5 kDa antibacterial protein from the granular haemocytes of the shore crab, Carcinus maenas

Extracts of the granular haemocytes of Carcinus maenas were subjected to ion-exchange chromatography and reverse-phase (RP)-HPLC to investigate the presence of an antibacterial protein of approximate to 11 kDa, This protein was isolated, characterized and subjected to partial amino acid sequence analysis. It was found by mass spectrometry to have a molecular mass of 11 534 Da, to be cationic and hydrophobic and active only against marine Gram-positive bacteria. In addition its activity is stable after heating to 100 degrees C and is retained at concentrations as low as 10 mu g.mL(-1). It has an unusual amino acid sequence, unlike any known antibacterial peptide described in the literature but bears a consensus disulphide domain signature, indicating that it might be a member of the four-disulphide core proteins. Partial cDNA sequence data has been obtained.</p